DSRAD_HUMAN
ID DSRAD_HUMAN Reviewed; 1226 AA.
AC P55265; B1AQQ9; B1AQR0; D3DV76; O15223; O43859; O43860; Q9BYM3; Q9BYM4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=Double-stranded RNA-specific adenosine deaminase;
DE Short=DRADA {ECO:0000303|PubMed:7972084};
DE EC=3.5.4.37 {ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:7972084};
DE AltName: Full=136 kDa double-stranded RNA-binding protein;
DE Short=p136;
DE AltName: Full=Interferon-inducible protein 4;
DE Short=IFI-4;
DE AltName: Full=K88DSRBP;
GN Name=ADAR; Synonyms=ADAR1, DSRAD, G1P1, IFI4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND VARIANT GLY-100.
RX PubMed=7972084; DOI=10.1073/pnas.91.24.11457;
RA Kim U., Wang Y., Sanford T., Zeng Y., Nishikura K.;
RT "Molecular cloning of cDNA for double-stranded RNA adenosine deaminase, a
RT candidate enzyme for nuclear RNA editing.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11457-11461(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, INDUCTION BY INTERFERON, AND VARIANTS GLY-100 AND
RP ARG-384.
RC TISSUE=Kidney;
RX PubMed=7565688; DOI=10.1128/mcb.15.10.5376;
RA Patterson J.B., Samuel C.E.;
RT "Expression and regulation by interferon of a double-stranded-RNA-specific
RT adenosine deaminase from human cells: evidence for two forms of the
RT deaminase.";
RL Mol. Cell. Biol. 15:5376-5388(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP GLY-100 AND ARG-384.
RC TISSUE=Placenta;
RX PubMed=9020165; DOI=10.1074/jbc.272.7.4419;
RA Liu Y., George C.X., Patterson J.B., Samuel C.E.;
RT "Functionally distinct double-stranded RNA-binding domains associated with
RT alternative splice site variants of the interferon-inducible double-
RT stranded RNA-specific adenosine deaminase.";
RL J. Biol. Chem. 272:4419-4428(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), AND VARIANTS GLY-100 AND
RP ARG-384.
RC TISSUE=Cervix carcinoma;
RA Deblandre G., Marinx O., Nols C., Defrance P., Berr P., Huez G., Caput D.;
RT "The gene coding for the interferon-inducible human dsRNA adenosine
RT deaminase is transcribed into several messengers specifying different
RT proteins.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANTS GLY-100
RP AND ARG-384.
RC TISSUE=Amygdala, and Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-100.
RC TISSUE=Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP ALTERNATIVE PROMOTER USAGE, AND INDUCTION.
RX PubMed=10200312; DOI=10.1073/pnas.96.8.4621;
RA George C.X., Samuel C.E.;
RT "Human RNA-specific adenosine deaminase ADAR1 transcripts possess
RT alternative exon 1 structures that initiate from different promoters, one
RT constitutively active and the other interferon inducible.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4621-4626(1999).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, HOMODIMERIZATION, AND SUBUNIT.
RX PubMed=12618436; DOI=10.1074/jbc.m213127200;
RA Cho D.-S.C., Yang W., Lee J.T., Shiekhattar R., Murray J.M., Nishikura K.;
RT "Requirement of dimerization for RNA editing activity of adenosine
RT deaminases acting on RNA.";
RL J. Biol. Chem. 278:17093-17102(2003).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=12665561; DOI=10.1242/jcs.00371;
RA Desterro J.M.P., Keegan L.P., Lafarga M., Berciano M.T., O'Connell M.,
RA Carmo-Fonseca M.;
RT "Dynamic association of RNA-editing enzymes with the nucleolus.";
RL J. Cell Sci. 116:1805-1818(2003).
RN [12]
RP FUNCTION.
RX PubMed=15556947; DOI=10.1074/jbc.m407876200;
RA Yang W., Wang Q., Howell K.L., Lee J.T., Cho D.-S.C., Murray J.M.,
RA Nishikura K.;
RT "ADAR1 RNA deaminase limits short interfering RNA efficacy in mammalian
RT cells.";
RL J. Biol. Chem. 280:3946-3953(2005).
RN [13]
RP FUNCTION.
RX PubMed=15858013; DOI=10.1128/jvi.79.10.6291-6298.2005;
RA Taylor D.R., Puig M., Darnell M.E., Mihalik K., Feinstone S.M.;
RT "New antiviral pathway that mediates hepatitis C virus replicon interferon
RT sensitivity through ADAR1.";
RL J. Virol. 79:6291-6298(2005).
RN [14]
RP FUNCTION, SUMOYLATION AT LYS-418, AND MUTAGENESIS OF LYS-418.
RX PubMed=16120648; DOI=10.1091/mbc.e05-06-0536;
RA Desterro J.M.P., Keegan L.P., Jaffray E., Hay R.T., O'Connell M.A.,
RA Carmo-Fonseca M.;
RT "SUMO-1 modification alters ADAR1 editing activity.";
RL Mol. Biol. Cell 16:5115-5126(2005).
RN [15]
RP INTERACTION WITH ILF2 AND ILF3.
RX PubMed=16055709; DOI=10.1128/mcb.25.16.6956-6963.2005;
RA Nie Y., Ding L., Kao P.N., Braun R., Yang J.-H.;
RT "ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-
RT mediated gene expression independently of RNA editing.";
RL Mol. Cell. Biol. 25:6956-6963(2005).
RN [16]
RP FUNCTION.
RX PubMed=16475990; DOI=10.1111/j.1365-2893.2005.00663.x;
RA Hartwig D., Schuette C., Warnecke J., Dorn I., Hennig H., Kirchner H.,
RA Schlenke P.;
RT "The large form of ADAR 1 is responsible for enhanced hepatitis delta virus
RT RNA editing in interferon-alpha-stimulated host cells.";
RL J. Viral Hepat. 13:150-157(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [19]
RP FUNCTION, AND INTERACTION WITH EIF2AK2.
RX PubMed=17079286; DOI=10.1128/jvi.01527-06;
RA Nie Y., Hammond G.L., Yang J.H.;
RT "Double-stranded RNA deaminase ADAR1 increases host susceptibility to virus
RT infection.";
RL J. Virol. 81:917-923(2007).
RN [20]
RP ALTERNATIVE SPLICING, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=18178553; DOI=10.1074/jbc.m708316200;
RA Cenci C., Barzotti R., Galeano F., Corbelli S., Rota R., Massimi L.,
RA Di Rocco C., O'Connell M.A., Gallo A.;
RT "Down-regulation of RNA editing in pediatric astrocytomas: ADAR2 editing
RT activity inhibits cell migration and proliferation.";
RL J. Biol. Chem. 283:7251-7260(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601; SER-614; SER-823 AND
RP SER-825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [23]
RP INTERACTION WITH UPF1, AND SUBCELLULAR LOCATION.
RX PubMed=18362360; DOI=10.1073/pnas.0710576105;
RA Agranat L., Raitskin O., Sperling J., Sperling R.;
RT "The editing enzyme ADAR1 and the mRNA surveillance protein hUpf1 interact
RT in the cell nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5028-5033(2008).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [25]
RP FUNCTION.
RX PubMed=19710021; DOI=10.1074/jbc.m109.045146;
RA Toth A.M., Li Z., Cattaneo R., Samuel C.E.;
RT "RNA-specific adenosine deaminase ADAR1 suppresses measles virus-induced
RT apoptosis and activation of protein kinase PKR.";
RL J. Biol. Chem. 284:29350-29356(2009).
RN [26]
RP FUNCTION, AND INTERACTION WITH EIF2AK2.
RX PubMed=19605474; DOI=10.1128/jvi.02457-08;
RA Clerzius G., Gelinas J.F., Daher A., Bonnet M., Meurs E.F., Gatignol A.;
RT "ADAR1 interacts with PKR during human immunodeficiency virus infection of
RT lymphocytes and contributes to viral replication.";
RL J. Virol. 83:10119-10128(2009).
RN [27]
RP SUBCELLULAR LOCATION, INTERACTION WITH TNPO1 AND XPO5, AND DOMAIN.
RX PubMed=19124606; DOI=10.1128/mcb.01519-08;
RA Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P.,
RA Jantsch M.F.;
RT "RNA-regulated interaction of transportin-1 and exportin-5 with the double-
RT stranded RNA-binding domain regulates nucleocytoplasmic shuttling of
RT ADAR1.";
RL Mol. Cell. Biol. 29:1487-1497(2009).
RN [28]
RP FUNCTION.
RX PubMed=19651874; DOI=10.1093/nar/gkp604;
RA Doria M., Neri F., Gallo A., Farace M.G., Michienzi A.;
RT "Editing of HIV-1 RNA by the double-stranded RNA deaminase ADAR1 stimulates
RT viral infection.";
RL Nucleic Acids Res. 37:5848-5858(2009).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-601 AND THR-808, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [30]
RP REVIEW.
RX PubMed=20192758; DOI=10.1146/annurev-biochem-060208-105251;
RA Nishikura K.;
RT "Functions and regulation of RNA editing by ADAR deaminases.";
RL Annu. Rev. Biochem. 79:321-349(2010).
RN [31]
RP FUNCTION.
RX PubMed=19908260; DOI=10.1002/ijc.25022;
RA Galeano F., Leroy A., Rossetti C., Gromova I., Gautier P., Keegan L.P.,
RA Massimi L., Di Rocco C., O'Connell M.A., Gallo A.;
RT "Human BLCAP transcript: new editing events in normal and cancerous
RT tissues.";
RL Int. J. Cancer 127:127-137(2010).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-808 AND SER-825, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [33]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [34]
RP REVIEW.
RX PubMed=22022963; DOI=10.1134/s0006297911080050;
RA Wang Q.;
RT "RNA editing catalyzed by ADAR1 and its function in mammalian cells.";
RL Biochemistry (Mosc.) 76:900-911(2011).
RN [35]
RP FUNCTION.
RX PubMed=21289159; DOI=10.1099/vir.0.028043-0;
RA Doria M., Tomaselli S., Neri F., Ciafre S.A., Farace M.G., Michienzi A.,
RA Gallo A.;
RT "ADAR2 editing enzyme is a novel human immunodeficiency virus-1 proviral
RT factor.";
RL J. Gen. Virol. 92:1228-1232(2011).
RN [36]
RP REVIEW.
RX PubMed=21182352; DOI=10.1089/jir.2010.0097;
RA George C.X., Gan Z., Liu Y., Samuel C.E.;
RT "Adenosine deaminases acting on RNA, RNA editing, and interferon action.";
RL J. Interferon Cytokine Res. 31:99-117(2011).
RN [37]
RP REVIEW.
RX PubMed=21490091; DOI=10.1128/jvi.00240-11;
RA Gelinas J.F., Clerzius G., Shaw E., Gatignol A.;
RT "Enhancement of replication of RNA viruses by ADAR1 via RNA editing and
RT inhibition of RNA-activated protein kinase.";
RL J. Virol. 85:8460-8466(2011).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [39]
RP REVIEW.
RX PubMed=21211811; DOI=10.1016/j.virol.2010.12.004;
RA Samuel C.E.;
RT "Adenosine deaminases acting on RNA (ADARs) are both antiviral and
RT proviral.";
RL Virology 411:180-193(2011).
RN [40]
RP REVIEW.
RX PubMed=22988838; DOI=10.3109/10409238.2012.714350;
RA Mallela A., Nishikura K.;
RT "A-to-I editing of protein coding and noncoding RNAs.";
RL Crit. Rev. Biochem. Mol. Biol. 47:493-501(2012).
RN [41]
RP REVIEW.
RX PubMed=21769729; DOI=10.1007/82_2011_144;
RA Goodman R.A., Macbeth M.R., Beal P.A.;
RT "ADAR proteins: structure and catalytic mechanism.";
RL Curr. Top. Microbiol. Immunol. 353:1-33(2012).
RN [42]
RP FUNCTION.
RX PubMed=22278222; DOI=10.1128/jvi.06307-11;
RA Li Z., Okonski K.M., Samuel C.E.;
RT "Adenosine deaminase acting on RNA 1 (ADAR1) suppresses the induction of
RT interferon by measles virus.";
RL J. Virol. 86:3787-3794(2012).
RN [43]
RP REVIEW.
RX PubMed=22113393; DOI=10.1007/s12035-011-8220-2;
RA Orlandi C., Barbon A., Barlati S.;
RT "Activity regulation of adenosine deaminases acting on RNA (ADARs).";
RL Mol. Neurobiol. 45:61-75(2012).
RN [44]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; THR-601; THR-603;
RP SER-629; SER-636; THR-808; SER-814 AND SER-825, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [45]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [46]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-26, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [47]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [48]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-418, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [49]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-384; LYS-408; LYS-418; LYS-580
RP AND LYS-875, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 133-209 IN COMPLEX WITH Z-DNA, AND
RP DOMAIN.
RX PubMed=10364558; DOI=10.1126/science.284.5421.1841;
RA Schwartz T., Rould M.A., Lowenhaupt K., Herbert A., Rich A.;
RT "Crystal structure of the Z alpha domain of the human editing enzyme ADAR1
RT bound to left-handed Z-DNA.";
RL Science 284:1841-1845(1999).
RN [51]
RP STRUCTURE BY NMR OF 125-201 IN COMPLEX WITH Z-DNA AND ALONE, AND DOMAIN.
RX PubMed=10535945; DOI=10.1073/pnas.96.22.12465;
RA Schade M., Turner C.J., Kuehne R., Schmieder P., Lowenhaupt K., Herbert A.,
RA Rich A., Oschkinat H.;
RT "The solution structure of the Zalpha domain of the human RNA editing
RT enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:12465-12470(1999).
RN [52] {ECO:0007744|PDB:2ACJ}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 140-202 IN COMPLEX WITH DNA, AND
RP DOMAIN.
RX PubMed=16237447; DOI=10.1038/nature04088;
RA Ha S.C., Lowenhaupt K., Rich A., Kim Y.G., Kim K.K.;
RT "Crystal structure of a junction between B-DNA and Z-DNA reveals two
RT extruded bases.";
RL Nature 437:1183-1186(2005).
RN [53]
RP STRUCTURE BY NMR OF 708-801, DOMAIN, SUBCELLULAR LOCATION, INTERACTION WITH
RP TNPO1, AND MUTAGENESIS OF 708-MET--PRO-710; 708-MET--ARG-801;
RP 712-LYS--LYS-715; 716-ILE--ASN-724; ILE-716; GLU-718; LEU-719; ARG-721;
RP LEU-723; ASN-724; 725-THR--ARG-801; 777-LYS-LYS-778 AND ARG-801.
RX PubMed=24753571; DOI=10.1073/pnas.1323698111;
RA Barraud P., Banerjee S., Mohamed W.I., Jantsch M.F., Allain F.H.;
RT "A bimodular nuclear localization signal assembled via an extended double-
RT stranded RNA-binding domain acts as an RNA-sensing signal for transportin
RT 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E1852-E1861(2014).
RN [54]
RP VARIANTS DSH PRO-923 AND SER-1165.
RX PubMed=12916015; DOI=10.1086/378209;
RA Miyamura Y., Suzuki T., Kono M., Inagaki K., Ito S., Suzuki N., Tomita Y.;
RT "Mutations of the RNA-specific adenosine deaminase gene (DSRAD) are
RT involved in dyschromatosis symmetrica hereditaria.";
RL Am. J. Hum. Genet. 73:693-699(2003).
RN [55]
RP VARIANT DSH PHE-966.
RX PubMed=15146470; DOI=10.1002/humu.9246;
RA Zhang X.-J., He P.-P., Li M., He C.-D., Yan K.-L., Cui Y., Yang S.,
RA Zhang K.-Y., Gao M., Chen J.-J., Li C.-R., Jin L., Chen H.-D., Xu S.-J.,
RA Huang W.;
RT "Seven novel mutations of the ADAR gene in Chinese families and sporadic
RT patients with dyschromatosis symmetrica hereditaria (DSH).";
RL Hum. Mutat. 23:629-630(2004).
RN [56]
RP VARIANT DSH TRP-1155.
RX PubMed=15659327; DOI=10.1016/j.jdermsci.2004.11.004;
RA Li C.-R., Li M., Ma H.-J., Luo D., Yang L.-J., Wang D.-G., Zhu X.-H.,
RA Yue X.-Z., Chen W.-Q., Zhu W.-Y.;
RT "A new arginine substitution mutation of DSRAD gene in a Chinese family
RT with dyschromatosis symmetrica hereditaria.";
RL J. Dermatol. Sci. 37:95-99(2005).
RN [57]
RP VARIANT [LARGE SCALE ANALYSIS] VAL-806.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [58]
RP VARIANTS AGS6 ALA-193; THR-870; THR-872; HIS-892; ASN-999; ARG-1007;
RP PHE-1112 AND HIS-1113.
RX PubMed=23001123; DOI=10.1038/ng.2414;
RA Rice G.I., Kasher P.R., Forte G.M., Mannion N.M., Greenwood S.M.,
RA Szynkiewicz M., Dickerson J.E., Bhaskar S.S., Zampini M., Briggs T.A.,
RA Jenkinson E.M., Bacino C.A., Battini R., Bertini E., Brogan P.A.,
RA Brueton L.A., Carpanelli M., De Laet C., de Lonlay P., del Toro M.,
RA Desguerre I., Fazzi E., Garcia-Cazorla A., Heiberg A., Kawaguchi M.,
RA Kumar R., Lin J.P., Lourenco C.M., Male A.M., Marques W. Jr., Mignot C.,
RA Olivieri I., Orcesi S., Prabhakar P., Rasmussen M., Robinson R.A.,
RA Rozenberg F., Schmidt J.L., Steindl K., Tan T.Y., van der Merwe W.G.,
RA Vanderver A., Vassallo G., Wakeling E.L., Wassmer E., Whittaker E.,
RA Livingston J.H., Lebon P., Suzuki T., McLaughlin P.J., Keegan L.P.,
RA O'Connell M.A., Lovell S.C., Crow Y.J.;
RT "Mutations in ADAR1 cause Aicardi-Goutieres syndrome associated with a type
RT I interferon signature.";
RL Nat. Genet. 44:1243-1248(2012).
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of adenosine to inosine
CC in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing
CC (PubMed:7972084, PubMed:7565688, PubMed:12618436). This may affect gene
CC expression and function in a number of ways that include mRNA
CC translation by changing codons and hence the amino acid sequence of
CC proteins since the translational machinery read the inosine as a
CC guanosine; pre-mRNA splicing by altering splice site recognition
CC sequences; RNA stability by changing sequences involved in nuclease
CC recognition; genetic stability in the case of RNA virus genomes by
CC changing sequences during viral RNA replication; and RNA structure-
CC dependent activities such as microRNA production or targeting or
CC protein-RNA interactions. Can edit both viral and cellular RNAs and can
CC edit RNAs at multiple sites (hyper-editing) or at specific sites (site-
CC specific editing). Its cellular RNA substrates include: bladder cancer-
CC associated protein (BLCAP), neurotransmitter receptors for glutamate
CC (GRIA2) and serotonin (HTR2C) and GABA receptor (GABRA3). Site-specific
CC RNA editing of transcripts encoding these proteins results in amino
CC acid substitutions which consequently alters their functional
CC activities. Exhibits low-level editing at the GRIA2 Q/R site, but edits
CC efficiently at the R/G site and HOTSPOT1. Its viral RNA substrates
CC include: hepatitis C virus (HCV), vesicular stomatitis virus (VSV),
CC measles virus (MV), hepatitis delta virus (HDV), and human
CC immunodeficiency virus type 1 (HIV-1). Exhibits either a proviral (HDV,
CC MV, VSV and HIV-1) or an antiviral effect (HCV) and this can be
CC editing-dependent (HDV and HCV), editing-independent (VSV and MV) or
CC both (HIV-1). Impairs HCV replication via RNA editing at multiple
CC sites. Enhances the replication of MV, VSV and HIV-1 through an
CC editing-independent mechanism via suppression of EIF2AK2/PKR activation
CC and function. Stimulates both the release and infectivity of HIV-1
CC viral particles by an editing-dependent mechanism where it associates
CC with viral RNAs and edits adenosines in the 5'UTR and the Rev and Tat
CC coding sequence. Can enhance viral replication of HDV via A-to-I
CC editing at a site designated as amber/W, thereby changing an UAG amber
CC stop codon to an UIG tryptophan (W) codon that permits synthesis of the
CC large delta antigen (L-HDAg) which has a key role in the assembly of
CC viral particles. However, high levels of ADAR1 inhibit HDV replication.
CC {ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:15556947,
CC ECO:0000269|PubMed:15858013, ECO:0000269|PubMed:16120648,
CC ECO:0000269|PubMed:16475990, ECO:0000269|PubMed:17079286,
CC ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:19651874,
CC ECO:0000269|PubMed:19710021, ECO:0000269|PubMed:19908260,
CC ECO:0000269|PubMed:21289159, ECO:0000269|PubMed:22278222,
CC ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:7972084}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine in double-stranded RNA + H(+) + H2O = inosine in
CC double-stranded RNA + NH4(+); Xref=Rhea:RHEA:10120, Rhea:RHEA-
CC COMP:13885, Rhea:RHEA-COMP:13886, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:82852; EC=3.5.4.37;
CC Evidence={ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:7565688,
CC ECO:0000269|PubMed:7972084};
CC -!- SUBUNIT: Homodimer. Homodimerization is essential for its catalytic
CC activity (PubMed:12618436). Isoform 5 can form heterodimers with
CC ADARB1/ADAR2. Isoform 1 interacts with ILF2/NF45 and ILF3/NF90
CC (PubMed:16055709). Binding to ILF3/NF90 up-regulates ILF3-mediated gene
CC expression. Isoform 1 and isoform 5 (via DRBM 3 domain) interact with
CC TNPO1 (PubMed:19124606, PubMed:24753571). Isoform 5 (via DRBM domains)
CC interacts with XPO5 (PubMed:19124606). Isoform 1 and isoform 5 can
CC interact with EIF2AK2/PKR and UPF1 (PubMed:17079286, PubMed:18362360).
CC {ECO:0000269|PubMed:10364558, ECO:0000269|PubMed:10535945,
CC ECO:0000269|PubMed:12618436, ECO:0000269|PubMed:16055709,
CC ECO:0000269|PubMed:17079286, ECO:0000269|PubMed:18178553,
CC ECO:0000269|PubMed:18362360, ECO:0000269|PubMed:19124606,
CC ECO:0000269|PubMed:19605474, ECO:0000269|PubMed:24753571}.
CC -!- INTERACTION:
CC P55265; Q13148: TARDBP; NbExp=3; IntAct=EBI-2462104, EBI-372899;
CC P55265; Q92900: UPF1; NbExp=3; IntAct=EBI-2462104, EBI-373471;
CC P55265; P03496: NS; Xeno; NbExp=8; IntAct=EBI-2462104, EBI-2547442;
CC P55265; PRO_0000037965 [P14340]; Xeno; NbExp=2; IntAct=EBI-2462104, EBI-9825968;
CC P55265; PRO_0000045599 [Q99IB8]; Xeno; NbExp=3; IntAct=EBI-2462104, EBI-6858501;
CC P55265-1; Q9UPY3: DICER1; NbExp=4; IntAct=EBI-6913056, EBI-395506;
CC P55265-1; Q15633: TARBP2; NbExp=2; IntAct=EBI-6913056, EBI-978581;
CC P55265-5; Q9UPY3: DICER1; NbExp=8; IntAct=EBI-6913210, EBI-395506;
CC P55265-5; Q15633: TARBP2; NbExp=3; IntAct=EBI-6913210, EBI-978581;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:7565688}. Nucleus {ECO:0000269|PubMed:24753571,
CC ECO:0000269|PubMed:7565688}. Note=Shuttles between the cytoplasm and
CC nucleus (PubMed:7565688, PubMed:24753571). Nuclear import is mediated
CC by TNPO1 (PubMed:24753571). {ECO:0000269|PubMed:24753571,
CC ECO:0000269|PubMed:7565688}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm
CC {ECO:0000269|PubMed:19124606}. Nucleus {ECO:0000269|PubMed:19124606,
CC ECO:0000269|PubMed:7565688}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12665561}. Note=Predominantly nuclear but can
CC shuttle between nucleus and cytoplasm. TNPO1 can mediate its nuclear
CC import whereas XPO5 can mediate its nuclear export.
CC {ECO:0000269|PubMed:19124606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=ADAR-a, ADAR1L, p150;
CC IsoId=P55265-1; Sequence=Displayed;
CC Name=2; Synonyms=ADAR-b;
CC IsoId=P55265-2; Sequence=VSP_008874;
CC Name=3; Synonyms=ADAR-c;
CC IsoId=P55265-3; Sequence=VSP_008873, VSP_008874;
CC Name=4;
CC IsoId=P55265-4; Sequence=VSP_008872;
CC Name=5; Synonyms=ADAR1S, p110;
CC IsoId=P55265-5; Sequence=VSP_019235;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, highest levels were found
CC in brain and lung (PubMed:7972084). Isoform 5 is expressed at higher
CC levels in astrocytomas as compared to normal brain tissue and
CC expression increases strikingly with the severity of the tumor, being
CC higher in the most aggressive tumors. {ECO:0000269|PubMed:18178553,
CC ECO:0000269|PubMed:7972084}.
CC -!- INDUCTION: Isoform 1 is induced by interferon alpha. Isoform 5 is
CC constitutively expressed. {ECO:0000269|PubMed:10200312,
CC ECO:0000269|PubMed:7565688}.
CC -!- DOMAIN: The third dsRNA-binding domain (DRBM 3) contains an additional
CC N-terminal alpha-helix that is part of a bi-partite nuclear
CC localization signal, together with the sequence immediately C-terminal
CC to DRBM 3. The presence of DRBM 3 is important to bring together the N-
CC terminal and the C-terminal part of the bi-partite nuclear localization
CC signal for import mediated by TNPO1 (PubMed:24753571). RNA binding
CC interferes with nuclear import (PubMed:19124606, PubMed:24753571).
CC {ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:24753571}.
CC -!- DOMAIN: The first Z-binding domain binds Z-DNA. {ECO:0000255|PROSITE-
CC ProRule:PRU00073, ECO:0000269|PubMed:10364558,
CC ECO:0000269|PubMed:10535945, ECO:0000269|PubMed:16237447}.
CC -!- PTM: Sumoylation reduces RNA-editing activity.
CC {ECO:0000269|PubMed:16120648}.
CC -!- DISEASE: Dyschromatosis symmetrica hereditaria (DSH) [MIM:127400]: An
CC autosomal dominant pigmentary genodermatosis characterized by a mixture
CC of hyperpigmented and hypopigmented macules distributed on the face and
CC the dorsal parts of the hands and feet, that appear in infancy or early
CC childhood. {ECO:0000269|PubMed:12916015, ECO:0000269|PubMed:15146470,
CC ECO:0000269|PubMed:15659327}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Aicardi-Goutieres syndrome 6 (AGS6) [MIM:615010]: A form of
CC Aicardi-Goutieres syndrome, a genetically heterogeneous disease
CC characterized by cerebral atrophy, leukoencephalopathy, intracranial
CC calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis,
CC increased CSF alpha-interferon, and negative serologic investigations
CC for common prenatal infection. Clinical features as thrombocytopenia,
CC hepatosplenomegaly and elevated hepatic transaminases along with
CC intermittent fever may erroneously suggest an infective process. Severe
CC neurological dysfunctions manifest in infancy as progressive
CC microcephaly, spasticity, dystonic posturing and profound psychomotor
CC retardation. Death often occurs in early childhood.
CC {ECO:0000269|PubMed:23001123}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- CAUTION: The N-terminus of isoform 4 has been derived from EST and
CC genomic sequences. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE45853.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U10439; AAB06697.1; -; mRNA.
DR EMBL; U75503; AAB97116.1; -; Genomic_DNA.
DR EMBL; U75489; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75490; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75491; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75492; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75493; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75494; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75495; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75496; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75497; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75498; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75499; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75500; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75501; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75502; AAB97116.1; JOINED; Genomic_DNA.
DR EMBL; U75503; AAB97117.1; -; Genomic_DNA.
DR EMBL; U75489; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75490; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75491; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75492; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75493; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75494; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75495; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75496; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75497; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75498; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75499; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75500; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75501; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75502; AAB97117.1; JOINED; Genomic_DNA.
DR EMBL; U75503; AAB97118.1; -; Genomic_DNA.
DR EMBL; U75489; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75490; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75491; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75492; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75493; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75494; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75495; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75496; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75497; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75498; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75499; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75500; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75501; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U75502; AAB97118.1; JOINED; Genomic_DNA.
DR EMBL; U18121; AAC13782.1; -; mRNA.
DR EMBL; X79448; CAA55967.1; -; mRNA.
DR EMBL; X79449; CAA55968.1; -; mRNA.
DR EMBL; X98559; CAA67169.1; -; mRNA.
DR EMBL; X98559; CAA67170.1; -; mRNA.
DR EMBL; BX538232; CAD98075.1; -; mRNA.
DR EMBL; BX640741; CAE45853.1; ALT_SEQ; mRNA.
DR EMBL; AL592078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53183.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53187.1; -; Genomic_DNA.
DR EMBL; BC038227; AAH38227.1; -; mRNA.
DR CCDS; CCDS1071.1; -. [P55265-1]
DR CCDS; CCDS30879.1; -. [P55265-5]
DR PIR; S65593; S65593.
DR RefSeq; NP_001020278.1; NM_001025107.2. [P55265-5]
DR RefSeq; NP_001102.2; NM_001111.4. [P55265-1]
DR RefSeq; NP_001180424.1; NM_001193495.1. [P55265-5]
DR RefSeq; NP_056655.2; NM_015840.3. [P55265-2]
DR RefSeq; NP_056656.2; NM_015841.3. [P55265-3]
DR RefSeq; XP_006711174.1; XM_006711111.3.
DR RefSeq; XP_006711175.1; XM_006711112.2.
DR RefSeq; XP_006711176.1; XM_006711113.2. [P55265-5]
DR PDB; 1QBJ; X-ray; 2.10 A; A/B/C=133-209.
DR PDB; 1QGP; NMR; -; A=125-200.
DR PDB; 1XMK; X-ray; 0.97 A; A=294-366.
DR PDB; 2ACJ; X-ray; 2.60 A; A/B/C/D=140-202.
DR PDB; 2GXB; X-ray; 2.25 A; A/B=140-202.
DR PDB; 2L54; NMR; -; A=136-198.
DR PDB; 2MDR; NMR; -; A=708-801.
DR PDB; 3F21; X-ray; 2.20 A; A/B/C=133-209.
DR PDB; 3F22; X-ray; 2.50 A; A/B/C=133-209.
DR PDB; 3F23; X-ray; 2.70 A; A/B/C=133-209.
DR PDB; 3IRQ; X-ray; 2.80 A; A/B/C/D=140-202.
DR PDB; 3IRR; X-ray; 2.65 A; A/B/C/D=140-202.
DR PDB; 5ZU1; X-ray; 3.01 A; A/B/C/D=140-198.
DR PDB; 5ZUO; X-ray; 2.90 A; A/B/C/D=140-202.
DR PDB; 5ZUP; X-ray; 2.90 A; A/B/C/D=140-202.
DR PDB; 7C0I; X-ray; 2.40 A; A/B/C=170-184.
DR PDBsum; 1QBJ; -.
DR PDBsum; 1QGP; -.
DR PDBsum; 1XMK; -.
DR PDBsum; 2ACJ; -.
DR PDBsum; 2GXB; -.
DR PDBsum; 2L54; -.
DR PDBsum; 2MDR; -.
DR PDBsum; 3F21; -.
DR PDBsum; 3F22; -.
DR PDBsum; 3F23; -.
DR PDBsum; 3IRQ; -.
DR PDBsum; 3IRR; -.
DR PDBsum; 5ZU1; -.
DR PDBsum; 5ZUO; -.
DR PDBsum; 5ZUP; -.
DR PDBsum; 7C0I; -.
DR AlphaFoldDB; P55265; -.
DR SMR; P55265; -.
DR BioGRID; 106617; 169.
DR CORUM; P55265; -.
DR DIP; DIP-29310N; -.
DR IntAct; P55265; 76.
DR MINT; P55265; -.
DR STRING; 9606.ENSP00000357459; -.
DR GlyGen; P55265; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; P55265; -.
DR MetOSite; P55265; -.
DR PhosphoSitePlus; P55265; -.
DR SwissPalm; P55265; -.
DR BioMuta; ADAR; -.
DR DMDM; 313104303; -.
DR EPD; P55265; -.
DR jPOST; P55265; -.
DR MassIVE; P55265; -.
DR MaxQB; P55265; -.
DR PaxDb; P55265; -.
DR PeptideAtlas; P55265; -.
DR PRIDE; P55265; -.
DR ProteomicsDB; 56826; -. [P55265-1]
DR ProteomicsDB; 56827; -. [P55265-2]
DR ProteomicsDB; 56828; -. [P55265-3]
DR ProteomicsDB; 56829; -. [P55265-4]
DR ProteomicsDB; 56830; -. [P55265-5]
DR Antibodypedia; 1280; 285 antibodies from 32 providers.
DR DNASU; 103; -.
DR Ensembl; ENST00000368471.8; ENSP00000357456.3; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000368474.9; ENSP00000357459.4; ENSG00000160710.18. [P55265-1]
DR Ensembl; ENST00000529168.2; ENSP00000431794.2; ENSG00000160710.18. [P55265-2]
DR Ensembl; ENST00000648231.2; ENSP00000497555.1; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000648311.1; ENSP00000498137.1; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000649022.2; ENSP00000496896.2; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000649042.1; ENSP00000497790.1; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000649724.1; ENSP00000497932.1; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000649749.1; ENSP00000497210.1; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000680270.1; ENSP00000505532.1; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000681056.1; ENSP00000506234.1; ENSG00000160710.18. [P55265-5]
DR Ensembl; ENST00000681683.1; ENSP00000506666.1; ENSG00000160710.18. [P55265-5]
DR GeneID; 103; -.
DR KEGG; hsa:103; -.
DR MANE-Select; ENST00000368474.9; ENSP00000357459.4; NM_001111.5; NP_001102.3.
DR UCSC; uc001ffh.4; human. [P55265-1]
DR CTD; 103; -.
DR DisGeNET; 103; -.
DR GeneCards; ADAR; -.
DR GeneReviews; ADAR; -.
DR HGNC; HGNC:225; ADAR.
DR HPA; ENSG00000160710; Low tissue specificity.
DR MalaCards; ADAR; -.
DR MIM; 127400; phenotype.
DR MIM; 146920; gene.
DR MIM; 615010; phenotype.
DR neXtProt; NX_P55265; -.
DR OpenTargets; ENSG00000160710; -.
DR Orphanet; 51; Aicardi-Goutieres syndrome.
DR Orphanet; 41; Dyschromatosis symmetrica hereditaria.
DR Orphanet; 225154; Familial infantile bilateral striatal necrosis.
DR PharmGKB; PA24555; -.
DR VEuPathDB; HostDB:ENSG00000160710; -.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000157243; -.
DR HOGENOM; CLU_005382_0_0_1; -.
DR InParanoid; P55265; -.
DR OMA; MQMRLKA; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; P55265; -.
DR TreeFam; TF315806; -.
DR BRENDA; 3.5.4.37; 2681.
DR PathwayCommons; P55265; -.
DR Reactome; R-HSA-75102; C6 deamination of adenosine.
DR Reactome; R-HSA-77042; Formation of editosomes by ADAR proteins.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR SignaLink; P55265; -.
DR SIGNOR; P55265; -.
DR BioGRID-ORCS; 103; 284 hits in 1085 CRISPR screens.
DR ChiTaRS; ADAR; human.
DR EvolutionaryTrace; P55265; -.
DR GeneWiki; ADAR; -.
DR GenomeRNAi; 103; -.
DR Pharos; P55265; Tbio.
DR PRO; PR:P55265; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P55265; protein.
DR Bgee; ENSG00000160710; Expressed in endothelial cell and 208 other tissues.
DR ExpressionAtlas; P55265; baseline and differential.
DR Genevisible; P55265; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0044530; C:supraspliceosomal complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IDA:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0006382; P:adenosine to inosine editing; IDA:UniProtKB.
DR GO; GO:0016553; P:base conversion or substitution editing; IDA:MGI.
DR GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:1900369; P:negative regulation of post-transcriptional gene silencing by RNA; IEA:Ensembl.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IDA:UniProtKB.
DR GO; GO:0031054; P:pre-miRNA processing; IDA:MGI.
DR GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; IDA:UniProtKB.
DR GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IMP:UniProtKB.
DR GO; GO:0070922; P:RISC complex assembly; IDA:MGI.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0002566; P:somatic diversification of immune receptors via somatic mutation; IEA:Ensembl.
DR CDD; cd19913; DSRM_DRADA_rpt1; 1.
DR CDD; cd19915; DSRM_DRADA_rpt3; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR044456; ADAR1_DSRM_1.
DR InterPro; IPR044457; ADAR1_DSRM_3.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR042371; Z_dom.
DR Pfam; PF02137; A_deamin; 1.
DR Pfam; PF00035; dsrm; 3.
DR Pfam; PF02295; z-alpha; 2.
DR SMART; SM00552; ADEAMc; 1.
DR SMART; SM00358; DSRM; 3.
DR SMART; SM00550; Zalpha; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50137; DS_RBD; 3.
DR PROSITE; PS50139; Z_BINDING; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Aicardi-Goutieres syndrome; Alternative promoter usage;
KW Alternative splicing; Antiviral defense; Cytoplasm;
KW Direct protein sequencing; Disease variant; DNA-binding; Hydrolase;
KW Immunity; Innate immunity; Isopeptide bond; Metal-binding; Methylation;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing; Ubl conjugation; Zinc.
FT CHAIN 1..1226
FT /note="Double-stranded RNA-specific adenosine deaminase"
FT /id="PRO_0000171774"
FT DOMAIN 133..199
FT /note="Z-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00073,
FT ECO:0000269|PubMed:10364558, ECO:0000269|PubMed:10535945,
FT ECO:0000269|PubMed:16237447"
FT DOMAIN 293..357
FT /note="Z-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00073"
FT DOMAIN 503..571
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 614..682
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 726..794
FT /note="DRBM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266,
FT ECO:0000269|PubMed:24753571"
FT DOMAIN 886..1221
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 133..202
FT /note="Interaction with Z-DNA"
FT /evidence="ECO:0000269|PubMed:10364558,
FT ECO:0000269|PubMed:10535945, ECO:0000269|PubMed:16237447"
FT REGION 208..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..725
FT /note="N-terminal extension of DRBM 3 and constituent of a
FT bi-partite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24753571"
FT REGION 795..801
FT /note="C-terminal extension of DRBM 3 and constituent of a
FT bi-partite nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24753571"
FT COMPBIAS 574..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 912
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 966
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 1036
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT MOD_RES 26
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55266"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 601
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 603
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 614
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 823
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 384
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 580
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 875
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..295
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_019235"
FT VAR_SEQ 1..5
FT /note="MNPRQ -> MMSPICDQTIDSRLKVEKATWWGRVGGGSRPHWQPPGVRPCPE
FT EVQDP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008872"
FT VAR_SEQ 694..712
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_008873"
FT VAR_SEQ 807..832
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_008874"
FT VARIANT 100
FT /note="R -> G (in dbSNP:rs1466731)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005, ECO:0000269|PubMed:7565688,
FT ECO:0000269|PubMed:7972084, ECO:0000269|PubMed:9020165,
FT ECO:0000269|Ref.4"
FT /id="VAR_048725"
FT VARIANT 193
FT /note="P -> A (in AGS6; dbSNP:rs145588689)"
FT /evidence="ECO:0000269|PubMed:23001123"
FT /id="VAR_069535"
FT VARIANT 384
FT /note="K -> R (in dbSNP:rs2229857)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:7565688, ECO:0000269|PubMed:9020165,
FT ECO:0000269|Ref.4"
FT /id="VAR_017240"
FT VARIANT 587
FT /note="Y -> C (in dbSNP:rs17843865)"
FT /id="VAR_024407"
FT VARIANT 806
FT /note="E -> V (in a breast cancer sample; somatic mutation;
FT dbSNP:rs144119808)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035805"
FT VARIANT 870
FT /note="A -> T (in AGS6; dbSNP:rs398122893)"
FT /evidence="ECO:0000269|PubMed:23001123"
FT /id="VAR_069536"
FT VARIANT 872
FT /note="I -> T (in AGS6; dbSNP:rs398122897)"
FT /evidence="ECO:0000269|PubMed:23001123"
FT /id="VAR_069537"
FT VARIANT 892
FT /note="R -> H (in AGS6; dbSNP:rs398122892)"
FT /evidence="ECO:0000269|PubMed:23001123"
FT /id="VAR_069538"
FT VARIANT 923
FT /note="L -> P (in DSH; dbSNP:rs28936680)"
FT /evidence="ECO:0000269|PubMed:12916015"
FT /id="VAR_017604"
FT VARIANT 966
FT /note="C -> F (in DSH)"
FT /evidence="ECO:0000269|PubMed:15146470"
FT /id="VAR_021729"
FT VARIANT 999
FT /note="K -> N (in AGS6; dbSNP:rs398122896)"
FT /evidence="ECO:0000269|PubMed:23001123"
FT /id="VAR_069539"
FT VARIANT 1007
FT /note="G -> R (in AGS6; dbSNP:rs398122822)"
FT /evidence="ECO:0000269|PubMed:23001123"
FT /id="VAR_069540"
FT VARIANT 1112
FT /note="Y -> F (in AGS6; dbSNP:rs398122895)"
FT /evidence="ECO:0000269|PubMed:23001123"
FT /id="VAR_069541"
FT VARIANT 1113
FT /note="D -> H (in AGS6; dbSNP:rs398122894)"
FT /evidence="ECO:0000269|PubMed:23001123"
FT /id="VAR_069542"
FT VARIANT 1155
FT /note="R -> W (in DSH; dbSNP:rs1044845711)"
FT /evidence="ECO:0000269|PubMed:15659327"
FT /id="VAR_026669"
FT VARIANT 1165
FT /note="F -> S (in DSH; dbSNP:rs28936681)"
FT /evidence="ECO:0000269|PubMed:12916015"
FT /id="VAR_017605"
FT MUTAGEN 418
FT /note="K->R: Abolishes sumoylation."
FT /evidence="ECO:0000269|PubMed:16120648"
FT MUTAGEN 708..801
FT /note="Missing: Abolishes nuclear location."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 708..710
FT /note="MMP->AMA: Decreased nuclear and partially
FT cytoplasmic location."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 712..715
FT /note="KVRK->AVAA: No effect on nuclear location. No effect
FT on RNA binding."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 716..724
FT /note="Missing: Disrupts the bi-partite nuclear
FT localization signal and abolishes nuclear location."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 716
FT /note="I->N: Disrupts the bi-partite nuclear localization
FT signal and abolishes nuclear location; when associated with
FT S-719 and N-723."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 718
FT /note="E->A: No effect on nuclear location; when associated
FT with A-721 and A-724."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 719
FT /note="L->S: Disrupts the bi-partite nuclear localization
FT signal and abolishes nuclear location; when associated with
FT N-716 and N-723."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 721
FT /note="R->A: No effect on nuclear location; when associated
FT with A-721 and A-724."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 723
FT /note="L->N: Disrupts the bi-partite nuclear localization
FT signal and abolishes nuclear location; when associated with
FT N-716 and S-719."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 724
FT /note="N->A: No effect on nuclear location; when associated
FT with A-718 and A-721."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 725..801
FT /note="Missing: Disrupts nuclear localization signal. No
FT effect on RNA binding."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 777..778
FT /note="KK->AA: Strongly impaired RNA binding. No effect on
FT nuclear location."
FT /evidence="ECO:0000269|PubMed:24753571"
FT MUTAGEN 801
FT /note="R->A: Abolishes interaction with TNPO1, TNPO1-
FT mediated nuclear import and nuclear location."
FT /evidence="ECO:0000269|PubMed:24753571"
FT CONFLICT 53
FT /note="E -> G (in Ref. 4; CAA55968)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="F -> L (in Ref. 5; CAE45853)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="F -> L (in Ref. 5; CAE45853)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="I -> V (in Ref. 5; CAE45853)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093
FT /note="D -> G (in Ref. 5; CAE45853)"
FT /evidence="ECO:0000305"
FT CONFLICT 1184
FT /note="E -> K (in Ref. 4; CAA55967/CAA55968/CAA67169/
FT CAA67170)"
FT /evidence="ECO:0000305"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1QGP"
FT HELIX 135..150
FT /evidence="ECO:0007829|PDB:1QBJ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1QGP"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:1QBJ"
FT HELIX 169..181
FT /evidence="ECO:0007829|PDB:1QBJ"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:1QBJ"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:1QBJ"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:1XMK"
FT HELIX 315..322
FT /evidence="ECO:0007829|PDB:1XMK"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1XMK"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:1XMK"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:1XMK"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1XMK"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:1XMK"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:1XMK"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:1XMK"
FT HELIX 716..724
FT /evidence="ECO:0007829|PDB:2MDR"
FT HELIX 727..738
FT /evidence="ECO:0007829|PDB:2MDR"
FT STRAND 742..749
FT /evidence="ECO:0007829|PDB:2MDR"
FT STRAND 758..764
FT /evidence="ECO:0007829|PDB:2MDR"
FT STRAND 767..776
FT /evidence="ECO:0007829|PDB:2MDR"
FT HELIX 777..796
FT /evidence="ECO:0007829|PDB:2MDR"
FT CONFLICT P55265-4:13
FT /note="R -> G (in Ref. 5; CAE45853)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1226 AA; 136066 MW; 9CE095D6F9C1BC79 CRC64;
MNPRQGYSLS GYYTHPFQGY EHRQLRYQQP GPGSSPSSFL LKQIEFLKGQ LPEAPVIGKQ
TPSLPPSLPG LRPRFPVLLA SSTRGRQVDI RGVPRGVHLR SQGLQRGFQH PSPRGRSLPQ
RGVDCLSSHF QELSIYQDQE QRILKFLEEL GEGKATTAHD LSGKLGTPKK EINRVLYSLA
KKGKLQKEAG TPPLWKIAVS TQAWNQHSGV VRPDGHSQGA PNSDPSLEPE DRNSTSVSED
LLEPFIAVSA QAWNQHSGVV RPDSHSQGSP NSDPGLEPED SNSTSALEDP LEFLDMAEIK
EKICDYLFNV SDSSALNLAK NIGLTKARDI NAVLIDMERQ GDVYRQGTTP PIWHLTDKKR
ERMQIKRNTN SVPETAPAAI PETKRNAEFL TCNIPTSNAS NNMVTTEKVE NGQEPVIKLE
NRQEARPEPA RLKPPVHYNG PSKAGYVDFE NGQWATDDIP DDLNSIRAAP GEFRAIMEMP
SFYSHGLPRC SPYKKLTECQ LKNPISGLLE YAQFASQTCE FNMIEQSGPP HEPRFKFQVV
INGREFPPAE AGSKKVAKQD AAMKAMTILL EEAKAKDSGK SEESSHYSTE KESEKTAESQ
TPTPSATSFF SGKSPVTTLL ECMHKLGNSC EFRLLSKEGP AHEPKFQYCV AVGAQTFPSV
SAPSKKVAKQ MAAEEAMKAL HGEATNSMAS DNQPEGMISE SLDNLESMMP NKVRKIGELV
RYLNTNPVGG LLEYARSHGF AAEFKLVDQS GPPHEPKFVY QAKVGGRWFP AVCAHSKKQG
KQEAADAALR VLIGENEKAE RMGFTEVTPV TGASLRRTML LLSRSPEAQP KTLPLTGSTF
HDQIAMLSHR CFNTLTNSFQ PSLLGRKILA AIIMKKDSED MGVVVSLGTG NRCVKGDSLS
LKGETVNDCH AEIISRRGFI RFLYSELMKY NSQTAKDSIF EPAKGGEKLQ IKKTVSFHLY
ISTAPCGDGA LFDKSCSDRA MESTESRHYP VFENPKQGKL RTKVENGEGT IPVESSDIVP
TWDGIRLGER LRTMSCSDKI LRWNVLGLQG ALLTHFLQPI YLKSVTLGYL FSQGHLTRAI
CCRVTRDGSA FEDGLRHPFI VNHPKVGRVS IYDSKRQSGK TKETSVNWCL ADGYDLEILD
GTRGTVDGPR NELSRVSKKN IFLLFKKLCS FRYRRDLLRL SYGEAKKAAR DYETAKNYFK
KGLKDMGYGN WISKPQEEKN FYLCPV
